Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Anthony M, Pedley"'
Publikováno v:
Annu Rev Biochem
Over the past fifteen years, we have unveiled a new mechanism by which cells achieve greater efficiency in de novo purine biosynthesis. This mechanism relies on the compartmentalization of de novo purine biosynthetic enzymes into a dynamic complex ca
Autor:
Chunliang Liu, Lewis C. Cantley, Jingxuan He, Giselle M. Knudsen, Stephen J. Benkovic, Tomer M. Yaron, Anthony M. Pedley, Jared L. Johnson
Publikováno v:
J Proteome Res
Purines represent a class of essential metabolites produced by the cell to maintain cellular homeostasis and facilitate cell proliferation. In times of high purine demand, the de novo purine biosynthetic pathway is activated; however, the mechanisms
Replication protein A dynamically regulates monoubiquitination of proliferating cell nuclear antigen
Publikováno v:
Journal of Biological Chemistry. 294:5157-5168
DNA damage tolerance permits bypass of DNA lesions encountered during S-phase and may be carried out by translesion DNA synthesis (TLS). Human TLS requires selective monoubiquitination of proliferating cell nuclear antigen (PCNA) sliding clamps encir
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e102481 (2014)
The expanding roles of PCNA in functional assembly of DNA replication and repair complexes motivated investigation of the structural and dynamic properties guiding specificity of PCNA-protein interactions. A series of biochemical and computational an
Externí odkaz:
https://doaj.org/article/bdbd0de490f540c2aaa01ee4a80a37cb
Autor:
Anthony M. Pedley, Jack P. Boylan, Chung Yu Chan, Erin L. Kennedy, Minjoung Kyoung, Stephen J. Benkovic
Publikováno v:
Journal of Biological Chemistry. 298:101845
Enzymes within the de novo purine biosynthetic pathway spatially organize into dynamic intracellular assemblies called purinosomes. The formation of purinosomes has been correlated with growth conditions resulting in high purine demand, and therefore
Publikováno v:
Crit Rev Biochem Mol Biol
The focus of this review is the human de novo purine biosynthetic pathway. The pathway enzymes are enumerated, as well as the reactions they catalyze and their physical properties. Early literature evidence suggested that they might assemble into a m
Autor:
Ali Tavassoli, Monika Papayova, Anthony M. Pedley, Cyrielle Doigneaux, Stephen J. Benkovic, Ishna N. Mistry
Publikováno v:
The Journal of Biological Chemistry
The purinosome is a dynamic metabolic complex composed of enzymes responsible for de novo purine biosynthesis, whose formation has been associated with elevated purine demand. However, the physiological conditions that govern purinosome formation in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c237184cb2ab8591bdc930620d2a157
https://eprints.soton.ac.uk/441089/
https://eprints.soton.ac.uk/441089/
Publikováno v:
Biochemistry. 57:3217-3221
Despite purines making up one of the largest classes of metabolites in a cell, little is known about the regulatory mechanisms that facilitate efficient purine production. Under conditions resulting in high purine demand, enzymes within the de novo p
Autor:
Michael K. Wendt, Remah Ali, Kyle E. Harvey, Vincent Jo Davisson, Anthony M. Pedley, Matthew D. Bartolowits, Wells S. Brown, Qingshou Chen
Publikováno v:
ACS Chemical Biology. 12:2371-2378
The discovery of compounds that selectively modulate signaling and effector proteins downstream of EGFR could have important implications for understanding specific roles for pathway activation. A complicating factor for receptor tyrosine kinases is
Autor:
Ye Fang, Stephen J. Benkovic, Haibei Hu, Huayun Deng, Jarrod B. French, Hong Zhao, Sara A. Jones, Doory Kim, Chung Yu Chan, Raymond J. Pugh, Xiaowei Zhuang, Anthony M. Pedley, Tony Jun Huang, Youxin Zhang
Publikováno v:
Science. 351:733-737
Spatial control of cellular enzymes Purine is a building block of DNA and also a component of ATP that is used as an energy source in the cell. Enzymes involved in purine biosynthesis organize into dynamic bodies called purinosomes. French et al. fou